Evidence map›Paper›PMID 25336651›Full record

ArticleThe Journal of biological chemistry2014

Novel RNA-binding protein P311 binds eukaryotic translation initiation factor 3 subunit b (eIF3b) to promote translation of transforming growth factor β1-3 (TGF-β1-3).

Michael M Yue, Kaosheng Lv, Stephen C Meredith, Jennifer L Martindale, Myriam Gorospe, Lucia Schuger

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Article
  2. Review
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  8. Review
  9. Article
  10. Common and Rare Genetic Variants That Could Contribute to Severe Otitis Media in an Australian Aboriginal Population.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. P311, a novel intrinsically disordered protein, regulates adipocyte development.Biochemical and biophysical research communications · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Michael M YueFrom the Departments of Pathology and.
Kaosheng LvFrom the Departments of Pathology and.
Stephen C MeredithFrom the Departments of Pathology and Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637 and.
Jennifer L Martindalethe Laboratory of Genetics, NIA, National Institutes of Health, Baltimore, Maryland 21224.
Myriam Gorospethe Laboratory of Genetics, NIA, National Institutes of Health, Baltimore, Maryland 21224.
Lucia SchugerFrom the Departments of Pathology and lschuger@bsd.uchicago.edu.

Funding

Post-transcriptional Regulation Of Proliferative and Stress Response GenesZIAAG000511 · NIA · NATIONAL INSTITUTE ON AGING · PI GOROSPE, MYRIAM · 2009 to 2025
$25.4M
Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Role of P311 in the development of skin hypertrophic scarsR01GM111116 · NIGMS · UNIVERSITY OF CHICAGO · PI SCHUGER, LUCIA · 2014 to 2017
$1.3M
NCATS NIH HHS UL1 TR000430NIGMS NIH HHS R01 GM111116NIGMS NIH HHS R01GM111116
6 · The paper itself

Abstract

P311, a conserved 8-kDa intracellular protein expressed in brain, smooth muscle, regenerating tissues, and malignant glioblastomas, represents the first documented stimulator of TGF-β1-3 translation in vitro and in vivo. Here we initiated efforts to define the mechanism underlying P311 function. PONDR® (Predictor Of Naturally Disordered Regions) analysis suggested and CD confirmed that P311 is an intrinsically disordered protein, therefore requiring an interacting partner to acquire tertiary structure and function. Immunoprecipitation coupled with mass spectroscopy identified eIF3 subunit b (eIF3b) as a novel P311 binding partner. Immunohistochemical colocalization, GST pulldown, and surface plasmon resonance studies revealed that P311-eIF3b interaction is direct and has a Kd of 1.26 μm. Binding sites were mapped to the non-canonical RNA recognition motif of eIF3b and a central 11-amino acid-long region of P311, here referred to as eIF3b binding motif. Disruption of P311-eIF3b binding inhibited translation of TGF-β1, 2, and 3, as indicated by luciferase reporter assays, polysome fractionation studies, and Western blot analysis. RNA precipitation assays after UV cross-linking and RNA-protein EMSA demonstrated that P311 binds directly to TGF-β 5'UTRs mRNAs through a previously unidentified RNA recognition motif-like motif. Our results demonstrate that P311 is a novel RNA-binding protein that, by interacting with TGF-βs 5'UTRs and eIF3b, stimulates the translation of TGF-β1, 2, and 3.

Indexed as

Protein Biosynthesis5' Untranslated RegionsAmino Acid SequenceAnimalsBinding SitesEscherichia coliEukaryotic Initiation Factor-3Gene Expression RegulationGenes, ReporterHumansLuciferasesMaleMiceMice, Inbred C57BLMolecular Sequence DataNerve Tissue Proteins5' Untranslated RegionsEIF3B protein, humanEukaryotic Initiation Factor-3LuciferasesNerve Tissue ProteinsNREP protein, humanOncogene ProteinsRecombinant ProteinsTransforming Growth Factor beta1Transforming Growth Factor beta2Transforming Growth Factor beta3mRNAProtein-Protein InteractionRNA-binding ProteinTransforming Growth Factor β (TGF-β)Translation Initiation Factor

Identifiers

PMID25336651
PMCPMC4256334

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.